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P22534

- GUNA_CALSA

UniProt

P22534 - GUNA_CALSA

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Protein

Endoglucanase A

Gene

celA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

The N-terminal domain of CelA codes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei396 – 3961By similarity
Active sitei434 – 4341By similarity
Active sitei443 – 4431By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH48. Glycoside Hydrolase Family 48.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene namesi
Name:celA
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 17421719Endoglucanase APRO_0000007944Add
BLAST

Post-translational modificationi

The linker region (also termed "hinge") may be a potential site for proteolysis.

Structurei

3D structure databases

ProteinModelPortaliP22534.
SMRiP22534. Positions 26-636, 1117-1739.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini477 – 637161CBM3 1PROSITE-ProRule annotationAdd
BLAST
Domaini703 – 856154CBM3 2PROSITE-ProRule annotationAdd
BLAST
Domaini906 – 1059154CBM3 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 476453Catalytic 1Add
BLAST
Regioni638 – 70265Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni857 – 90549Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni1060 – 111253Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni1113 – 1742630Catalytic 2Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family.Curated
Contains 3 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamiPF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM01067. CBM_3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEiPS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22534-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVVTFLFILG VVYGVKPWQE ARAGSFNYGE ALQKAIMFYE FQMSGKLPNW
60 70 80 90 100
VRNNWRGDSA LKDGQDNGLD LTGGWFDAGD HVKFNLPMSY TGTMLSWAAY
110 120 130 140 150
EYKDAFVKSG QLEHILNQIE WVNDYFVKCH PSKYVYYYQV GDGGKDHAWW
160 170 180 190 200
GPAEVMQMER PSFKVTQSSP GSAVVAETAA SLAAASIVLK DRNPTKAATY
210 220 230 240 250
LQHAKDLYEF AEVTKSDSGY TAANGYYNSW SGFYDELSWA AVWLYLATND
260 270 280 290 300
STYLTKAESY VQNWPKISGS NIIDYKWAHC WDDVHNGAAL LLAKITDKDT
310 320 330 340 350
YKQIIESHLD YWTTGYNGER IKYTPKGLAW LDQWGSLRYA TTTAFLAFVY
360 370 380 390 400
SDWSGCPTGK KETYRKFGES QIDYALGSTG RSFVVGFGTN PPKRPHHRTA
410 420 430 440 450
HSSWADSQSI PSYHRHTLYG ALVGGPGSDD SYTDDISNYV NNEVACDYNA
460 470 480 490 500
GFVGALAKMY LLYGGNPIPD FKAIETPTND EFFVEAGINA SGTNFIEIKA
510 520 530 540 550
IVNNQSGWPA RATNKLKFRY FVDLSELIKA GYSPNQLTLS TNYNQGAKVS
560 570 580 590 600
GPYVWDSSRN IYYILVDFTG TLIYPGGQDK YKKEVQFRIA APQNVQWDNS
610 620 630 640 650
NDYSFQDIKG VSSGSVVKTK YIPLYDEDIK VWGEEPGTSG VSPTPTASVT
660 670 680 690 700
PTPTPTPTAT PTPTPTPTVT PTPTVTATPT PTPTPTSTPT VTPTPTPVST
710 720 730 740 750
PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV
760 770 780 790 800
DGERAQSAIS DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ
810 820 830 840 850
PGKDTGEIQI RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV
860 870 880 890 900
WGQEPSGTTP APTSTPTVTV TPTPTPTPTV TPTPTVTATP TPTPTPTSTP
910 920 930 940 950
VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI DLSRVTIRYW
960 970 980 990 1000
YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG
1010 1020 1030 1040 1050
QLQPGKDTGE IQIRFNKDDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG
1060 1070 1080 1090 1100
VLVWGQEPSG ATPAPTVTPT PTVTPTPTPA PTPTATPTPT PTPTVTPTPT
1110 1120 1130 1140 1150
VAPTPTPSST PSGLGKYGQR FMWLWNKIHD PASGYFNQDG IPYHSVETLI
1160 1170 1180 1190 1200
CEAPDYGHLT TSEAFSYYVW LEAVYGKLTG DWSKFKTAWD TLEKYMIPSA
1210 1220 1230 1240 1250
EDQPMRSYDP NKPATYAGEW ETPDKYPSPL EFNVPVGKDP LHNELVSTYG
1260 1270 1280 1290 1300
STLMYGMHWL MDVDNWYGYG KRGDGVSRAS FINTFQRGPE ESVWETVPHP
1310 1320 1330 1340 1350
SWEEFKWGGP NGFLDLFIKD QNYSKQWRYT NAPDADARAI QATYWAKVWA
1360 1370 1380 1390 1400
KEQGKFNEIS SYVGKAAKMG DYLRYAMFDK YFKPLGCQDK NAAGGTGYDS
1410 1420 1430 1440 1450
AHYLLSWYYA WGGALDGAWS WKIGCSHAHF GYQNPMAAWA LANDSDMKPK
1460 1470 1480 1490 1500
SPNGASDWAK SLKRQIEFYR WLQSAEGAIA GGATNSWNGR YEKYPAGTAT
1510 1520 1530 1540 1550
FYGMAYEPNP VYRDPGSNTW FGFQAWSMQR VAEYYYVTGD KDAGTLLEKW
1560 1570 1580 1590 1600
VSWIKSVVKL NSDGTFAIPS TLDWSGQPDT WNGTYTGNPN LHVKVVDYGT
1610 1620 1630 1640 1650
DLGITASLAN ALLYYSAGTK KYGVFDEEAK NLAKELLDRM WKLYRDEKGL
1660 1670 1680 1690 1700
SAPEKRADYK RFFEQEVYIP AGWTGKMPNG DVIKSGVKFI DIRSKYKQDP
1710 1720 1730 1740
DWPKLEAAYK SGQVPEFRYH RFWAQCDIAI VNATYEILFG NQ
Length:1,742
Mass (Da):193,697
Last modified:October 1, 1996 - v2
Checksum:i3F0699A2123EED07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1545 – 15451T → A in AAA72860. (PubMed:2039230)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32742 Genomic DNA. Translation: AAA91086.1.
M36063 Genomic DNA. Translation: AAA72860.1.
L01257 Unassigned DNA. No translation available.
PIRiT17120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32742 Genomic DNA. Translation: AAA91086.1 .
M36063 Genomic DNA. Translation: AAA72860.1 .
L01257 Unassigned DNA. No translation available.
PIRi T17120.

3D structure databases

ProteinModelPortali P22534.
SMRi P22534. Positions 26-636, 1117-1739.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH48. Glycoside Hydrolase Family 48.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view ]
Pfami PF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
PRINTSi PR00844. GLHYDRLASE48.
SMARTi SM01067. CBM_3. 3 hits.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEi PS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum."
    Te'O V.S. Jr., Saul D.J., Bergquist P.L.
    Appl. Microbiol. Biotechnol. 43:291-296(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'."
    Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.
    Appl. Environ. Microbiol. 57:694-700(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742.

Entry informationi

Entry nameiGUNA_CALSA
AccessioniPrimary (citable) accession number: P22534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3